The Role of the Transmembrane RING Finger Proteins in Cellular and Organelle Function

Nakamura, Nobuhiro

doi:10.3390/membranes1040354

Cited by 79 publications

(83 citation statements)

References 254 publications

(349 reference statements)

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“…Among the RBR ubiquitin ligase family, there are five TMcontaining RBR proteins, including RNF19A (also named Dorfin), RNF19B (also named IBRDC3), RNF144A, RNF144B (also named IBRDC2 or p53RFP), and RNF217 (also named IBRDC1) (35). It has been shown that RNF19A requires both RBR and the TM domain to form high molecular weight forms that may be autoubiquitinated RNF19A (36).…”

Section: Discussionmentioning

confidence: 99%

Regulation of RNF144A E3 Ubiquitin Ligase Activity by Self-association through Its Transmembrane Domain

Lee

Lin

2015

Journal of Biological Chemistry

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Background: RNF144A is a membrane-associated E3 ubiquitin ligase. Results: The GXXXG motif within the TM domain of RNF144A mediates its self-association and activation of E3 ligase activity. Conclusion: The TM domain regulates RNF144A through two independent steps: membrane localization and GXXXG motifmediated self-association. Significance: The GXXXG motif is conserved among all RBR-TM proteins, suggesting a similar regulation for other RBR-TM proteins.

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Section: Discussionmentioning

confidence: 99%

Regulation of RNF144A E3 Ubiquitin Ligase Activity by Self-association through Its Transmembrane Domain

Lee

Lin

2015

Journal of Biological Chemistry

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“…Ubiquitylation of activated receptors is mediated by intracellular ubiquitin E3 ligases such as c-Cbl and Nedd4, although subsequent delivery steps are regulated by a series of ubiquitin-binding proteins [1,2]. cellular organelles and intracellular vesicles [4]. Of those, approximately 50 genes are predicted to encode transmembrane proteins, some of which show specific localization on intracellular membrane components, i.e.…”

Section: Introductionmentioning

confidence: 99%

“…The human genome harbours a large number of genes encoding ubiquitin E3 ligases (∼ 600 genes) [3], which mediate protein ubiquitylation to specific substrates. The PA-TM-RING family proteins are one subclass of the transmembrane-type ubiquitin ligases, and are composed of an N-terminal putative signal peptide, a PA (proteaseassociated) domain, a TM (transmembrane) domain, as well as a RING (really interesting new gene) domain [4,5]. cellular organelles and intracellular vesicles [4].…”

Section: Introductionmentioning

confidence: 99%

Tumour-associated mutations of PA-TM-RING ubiquitin ligases RNF167/RNF13 identify the PA domain as a determinant for endosomal localization

Dijk

Yamazaki

Palmer

2014

Biochemical Journal

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Diverse cellular processes depend on endocytosis, intracellular vesicle trafficking, sorting and exocytosis, and processes that are regulated post-transcriptionally by modifications such as phosphorylation and ubiquitylation. The PA (protease-associated) domain E3 ligases, such as GodzillaCG10277 in Drosophila melanogaster and RNF167 (RING finger protein 167) in humans, have been implicated in the regulation of cellular endosome trafficking. In the present study, we have characterized point mutations in the RING (really interesting new gene) domain of human RNF13 and RNF167, which have been identified in human tumour samples, that abrogate ubiquitin ligase activity as well as function. In the present study, we have also identified a functional role for the PA domain, which is required for endosomal localization of these proteins. Although the PA domain point mutations of RNF13 and RNF167 identified in human tumours are ligase active, the resultant mutant proteins are mislocalized within the cell. Thus the PA domain E3 ligases examined in the present study appear to require both E3 ligase activity as well as an intact PA domain to efficiently target and ubiquitylate their cellular substrates.

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“…We propose that the Asi ubiquitin ligase targets such mislocalised and potentially harmful proteins for degradation. Although the Asi proteins are not obviously conserved outside of yeast, the general importance of membrane-associated protein degradation mechanisms and the large diversity of integral membrane RING domain proteins in mammalian cells 29 suggest that dedicated E3 ubiquitin ligases functioning in INM-associated protein degradation probably exist in higher eukaryotes.…”

mentioning

confidence: 99%

Protein quality control at the inner nuclear membrane

Khmelinskii

Blaszczak

Pantazopoulou

et al. 2014

Nature

189

244

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The nuclear envelope is a double membrane that separates the nucleus from the cytoplasm. The inner nuclear membrane (INM) functions in essential nuclear processes including chromatin organization and regulation of gene expression1. The outer nuclear membrane is continuous with the endoplasmic reticulum (ER) and is the site of membrane protein synthesis. Protein homeostasis in this compartment is ensured by ER-associated protein degradation (ERAD) pathways that in yeast involve the integral membrane E3 ubiquitin ligases Hrd1 and Doa10 operating with the E2 ubiquitin-conjugating enzymes Ubc6 and Ubc72,3. However, little is known regarding protein quality control at the INM. Here we describe a protein degradation pathway at the INM mediated by the Asi complex consisting of the RING domain proteins Asi1 and Asi34. We report that the As complex functions together with the ubiquitin conjugating enzymes Ubc6andUbc7to degrade soluble and integral membrane proteins. Genetic evidence suggest that the Asi ubiquitin ligase defines a pathway distinct from but complementary to ERAD. Using unbiased screening with a novel genome-wide yeast library based on a tandem fluorescent protein timer (tFT)5, we identify more than 50 substrates of the Asi, Hrd1 and Doa10 E3 ubiquity ligases. We show that the Asi ubiquitin ligase is involved in degradation of mislocalised integral membrane proteins, thus acting to maintain and safeguard the identity of the INM.

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The Role of the Transmembrane RING Finger Proteins in Cellular and Organelle Function

Cited by 79 publications

References 254 publications

Regulation of RNF144A E3 Ubiquitin Ligase Activity by Self-association through Its Transmembrane Domain

Regulation of RNF144A E3 Ubiquitin Ligase Activity by Self-association through Its Transmembrane Domain

Tumour-associated mutations of PA-TM-RING ubiquitin ligases RNF167/RNF13 identify the PA domain as a determinant for endosomal localization

Protein quality control at the inner nuclear membrane

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